ID V9USE3_9PSED Unreviewed; 854 AA.
AC V9USE3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=X970_01525 {ECO:0000313|EMBL:AHC86134.1};
OS Pseudomonas monteilii SB3101.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC86134.1, ECO:0000313|Proteomes:UP000018660};
RN [1] {ECO:0000313|EMBL:AHC86134.1, ECO:0000313|Proteomes:UP000018660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3101 {ECO:0000313|EMBL:AHC86134.1,
RC ECO:0000313|Proteomes:UP000018660};
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA Nielsen J.L.;
RT "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP006979; AHC86134.1; -; Genomic_DNA.
DR RefSeq; WP_015268858.1; NC_023076.1.
DR AlphaFoldDB; V9USE3; -.
DR GeneID; 58533502; -.
DR KEGG; pmot:X970_01525; -.
DR PATRIC; fig|1435058.3.peg.293; -.
DR HOGENOM; CLU_005070_4_0_6; -.
DR Proteomes; UP000018660; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 854 AA; 94908 MW; A3F5F698610AB41F CRC64;
MRIDRLTSKL QLAISDAQSL AVGMDHPAIE PVHLLQALLE QQGGSIKPLL MQVGFDINSL
RQALVKELDQ LPKIQNPTGD VNMSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDENS
KLGKLLLSQG VSKKALENAI NNLRGGAAVN DANAEESRQA LDKYTVDLTK RAEEGKLDPV
IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPD GLKGKRLLAL
DMGALIAGAK YRGEFEERLK GLLNELSKQE GQIILFIDEL HTMVGAGKGE GAMDAGNMLK
PALARGELHC VGATTLNEYR QFIEKDAALE RRFQKVLVEE PSEEDTIAIL RGLKERYEVH
HKVAITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE VLDRLDRRLI
QLKVESQALK KEEDEAAKKR LEKLTEEIDR LEREYADLEE IWASEKAEVQ GSAQIQQKIE
QARQELETAR RKGDLSRMAE LQYGVIPDLE RSLQMVDQHG KTENQLLRNK VTEEEIAEVV
SKWTGIPVAK MLEGEREKLL KMEELLHQRV IGQNEAVTAV ANAVRRSRAG LSDPNRPSGS
FLFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSVVLLDEVE KAHPDVFNVL LQVLEDGRLT DSHGRTVDFR NTVIVMTSNL
GSAQIQELVG DREAQRAAVM DAVGSHFRPE FINRIDEVVV FEPLGREQIA GITEIQLGRL
RSRLLERELS LSLSPEALDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQL ILAGKFMPGT
AITAKVEGDE IVFG
//
